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R&D Systems cyclin b2

Loss of PAS1 Ccnb1 variant causes a delay in meiotic resumption. ( A ) Timing of GVBD in cultured denuded oocytes from WT and ΔPAS1 mutant mice. Oocytes were isolated as described in the Methods and timing of GVBD was scored by time-lapse microscopy after release from cilostamide block. Fifteen biological replicates for WT and six for the ΔPAS1 were included. Data were analyzed with non-parametric Mann–Whitney test and the calculated FDR was reported for each time point (* FDR ≤ 0.05; ** FDR ≤ 0.01; *** FDR ≤ 0.001). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT = 76.4 min, 95% confidence limit: 74.1–78.8; ΔPAS1 mutant = 107.4 min, 95% confidence limit: 96.2–120.1) as well as the slope of the curves (Hill coefficient: WT = 5.26, mutant = 3.99). ( B ) Timing of GVBD of individual oocytes from WT and ΔPAS1 mutant determined by time-lapse microscopy. Each point corresponded to one oocyte and the median of all determination was included. Statistical significance was calculated using unpaired t -test (**** P ≤ 0.0001). ( C ) Rescue of the PAS1 GVBD timing in ΔPAS1 oocytes. Denuded oocytes were microinjected with either vehicle (WT) or mRNA where the Ccnb1 ORF is fused to the intact PAS1 3′UTR ( Ccnb1 -PAS1 injected in ΔPAS1). The time when 50% of oocytes had undergone GVBD (Time 50% ) was comparable in the two groups (WT = 81.98 min; PAS1 rescue = 73.79). The two curves were not statistically different when using a Mann–Whitney test. ( D ) Representative immunoblots of <t>Cyclin</t> B1 and Cyclin <t>B2</t> levels in lysates of GV oocytes from WT and ΔPAS1 mutant mice (150 oocytes/lane). DDB1 was used as a loading control. ( E , F ) Quantification of (D), relative protein levels of Cyclin B1 and Cyclin B2 in GV oocytes from WT and PAS1 mutant. Three biological replicates were included. Statistical significance was assessed using unpaired t -test (**** P ≤ 0.0001, ns, not significant).

Cyclin B2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Alternative cleavage and polyadenylation of the Ccnb1 mRNA defines accumulation of cyclin protein during the meiotic cell cycle"

Article Title: Alternative cleavage and polyadenylation of the Ccnb1 mRNA defines accumulation of cyclin protein during the meiotic cell cycle

Journal: Nucleic Acids Research

doi: 10.1093/nar/gkad1151

Figure Legend Snippet: Loss of PAS1 Ccnb1 variant causes a delay in meiotic resumption. ( A ) Timing of GVBD in cultured denuded oocytes from WT and ΔPAS1 mutant mice. Oocytes were isolated as described in the Methods and timing of GVBD was scored by time-lapse microscopy after release from cilostamide block. Fifteen biological replicates for WT and six for the ΔPAS1 were included. Data were analyzed with non-parametric Mann–Whitney test and the calculated FDR was reported for each time point (* FDR ≤ 0.05; ** FDR ≤ 0.01; *** FDR ≤ 0.001). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT = 76.4 min, 95% confidence limit: 74.1–78.8; ΔPAS1 mutant = 107.4 min, 95% confidence limit: 96.2–120.1) as well as the slope of the curves (Hill coefficient: WT = 5.26, mutant = 3.99). ( B ) Timing of GVBD of individual oocytes from WT and ΔPAS1 mutant determined by time-lapse microscopy. Each point corresponded to one oocyte and the median of all determination was included. Statistical significance was calculated using unpaired t -test (**** P ≤ 0.0001). ( C ) Rescue of the PAS1 GVBD timing in ΔPAS1 oocytes. Denuded oocytes were microinjected with either vehicle (WT) or mRNA where the Ccnb1 ORF is fused to the intact PAS1 3′UTR ( Ccnb1 -PAS1 injected in ΔPAS1). The time when 50% of oocytes had undergone GVBD (Time 50% ) was comparable in the two groups (WT = 81.98 min; PAS1 rescue = 73.79). The two curves were not statistically different when using a Mann–Whitney test. ( D ) Representative immunoblots of Cyclin B1 and Cyclin B2 levels in lysates of GV oocytes from WT and ΔPAS1 mutant mice (150 oocytes/lane). DDB1 was used as a loading control. ( E , F ) Quantification of (D), relative protein levels of Cyclin B1 and Cyclin B2 in GV oocytes from WT and PAS1 mutant. Three biological replicates were included. Statistical significance was assessed using unpaired t -test (**** P ≤ 0.0001, ns, not significant).

Techniques Used: Variant Assay, Cell Culture, Mutagenesis, Isolation, Time-lapse Microscopy, Blocking Assay, MANN-WHITNEY, Injection, Western Blot, Control

Loss of PAS1 Ccnb1 variant does not affect mouse oocyte progression to MII. ( A ) Time-lapse microscopy analysis of timing of the first polar body extrusion in WT and PAS1 mutant oocytes after release from cilostamide block. Experiments were repeated 6 times with oocytes retrieved from at least 1 mouse/experiment. The two curves were not statistically different when using a Mann–Whitney test. Time 50% : WT = 11.0 min, 95% confidence limit: 10.88–11.20; ΔPAS1 = 12.48 min, 95% confidence limit:12.23–12.75. ( B ) Violin plot of the duration of the first meiotic division in WT and ΔPAS1 oocytes. The duration of the first meiotic division was calculated by subtracting the time of GVBD from the time of PB1 extrusion. Statistical significance was assessed using Mann–Whitney test (ns, not significant). Number of oocytes used for the measurements: WT n = 286, ΔPAS1 n = 143. ( C ) Representative immunoblot images of Cyclin B1 and pERK1/2 protein levels in metaphase II oocyte lysates from WT and ΔPAS1 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( D ) Quantifications of relative protein expression levels of Cyclin B1 (left) and pERK1/2 (right) in metaphase II oocytes of WT and ΔPAS1 from four biological replicates. Statistical significance was calculated using unpaired t -test (ns, not significant).

Figure Legend Snippet: Loss of PAS1 Ccnb1 variant does not affect mouse oocyte progression to MII. ( A ) Time-lapse microscopy analysis of timing of the first polar body extrusion in WT and PAS1 mutant oocytes after release from cilostamide block. Experiments were repeated 6 times with oocytes retrieved from at least 1 mouse/experiment. The two curves were not statistically different when using a Mann–Whitney test. Time 50% : WT = 11.0 min, 95% confidence limit: 10.88–11.20; ΔPAS1 = 12.48 min, 95% confidence limit:12.23–12.75. ( B ) Violin plot of the duration of the first meiotic division in WT and ΔPAS1 oocytes. The duration of the first meiotic division was calculated by subtracting the time of GVBD from the time of PB1 extrusion. Statistical significance was assessed using Mann–Whitney test (ns, not significant). Number of oocytes used for the measurements: WT n = 286, ΔPAS1 n = 143. ( C ) Representative immunoblot images of Cyclin B1 and pERK1/2 protein levels in metaphase II oocyte lysates from WT and ΔPAS1 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( D ) Quantifications of relative protein expression levels of Cyclin B1 (left) and pERK1/2 (right) in metaphase II oocytes of WT and ΔPAS1 from four biological replicates. Statistical significance was calculated using unpaired t -test (ns, not significant).

Techniques Used: Variant Assay, Time-lapse Microscopy, Mutagenesis, Blocking Assay, MANN-WHITNEY, Western Blot, Control, Expressing

Loss of PAS3 in the Ccnb1 3′ UTR leads to premature meiotic re-entry. ( A ) Time-lapse analysis of the timing of GVBD in WT and ΔPAS3 mutant oocytes after release from cilostamide block. Sixteen biological replicates for WT and five for the ΔPAS3 were included. Data were analyzed with non-parametric Mann–Whitney test and the calculated FDR was reported for each time point (*FDR ≤ 0.05; **FDR ≤ 0.01; ***FDR ≤ 0.001). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT = 76.06 min, 95% confidence limit: 72.6–79.6; ΔPAS3 = 50.20 min, 95% confidence limit: 47.92–52.63) as well as the slope of the curves (Hill coefficient: WT = 3.4, mutant = 7.8). ( B ) Representative immunoblot showing expression levels of Cyclin B1 and Cyclin B2 in WT and ΔPAS3 GV-stage oocyte lysates (150 oocytes/lane). DDB1 was used as a loading control. Quantifications of relative protein expression levels of Cyclin B1 (left) and Cyclin B2 (right) in GV-arrested oocytes from WT and ΔPAS3 mice from three biological replicates. Statistical significance was assessed using unpaired t-test (*** P ≤ 0.001, ns, not significant). ( C ) Overexpression of the intact Ccnb1 PAS1 short variant in WT oocytes causes premature meiotic cell cycle re-entry. WT oocytes were injected with an mRNA coding for PAS1 Ccnb1 short variant or a vehicle as a control. Timing of GVBD was assessed by time-lapse microscopy. Statistical significance was assessed using Mann–Whitney test (*** P ≤ 0.001, * P ≤ 0.05). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT + vehicle: 77.68 min, 95% confidence limit: 74.32–81.14; WT + Ccnb1 short: 57.38 min), as well as the slope of the curves (Hill coefficient: WT + vehicle: 4.0, WT + Ccnb1 short: 10). ( D ) Representative immunoblot showing the CDK1 activity in WT and ΔPAS3 oocytes 1 h after release from the cilostamide block (20 oocytes/lane). CDK1 activity was measured by phosphorylation level of the CDK1 substrate PP1 as detailed in the Materials and methods. Quantification of CDK1 activity levels between WT and PAS3 mutant from three biological replicates. Statistical significance was assessed using unpaired t -test (**** P ≤ 0.0001).

Figure Legend Snippet: Loss of PAS3 in the Ccnb1 3′ UTR leads to premature meiotic re-entry. ( A ) Time-lapse analysis of the timing of GVBD in WT and ΔPAS3 mutant oocytes after release from cilostamide block. Sixteen biological replicates for WT and five for the ΔPAS3 were included. Data were analyzed with non-parametric Mann–Whitney test and the calculated FDR was reported for each time point (*FDR ≤ 0.05; **FDR ≤ 0.01; ***FDR ≤ 0.001). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT = 76.06 min, 95% confidence limit: 72.6–79.6; ΔPAS3 = 50.20 min, 95% confidence limit: 47.92–52.63) as well as the slope of the curves (Hill coefficient: WT = 3.4, mutant = 7.8). ( B ) Representative immunoblot showing expression levels of Cyclin B1 and Cyclin B2 in WT and ΔPAS3 GV-stage oocyte lysates (150 oocytes/lane). DDB1 was used as a loading control. Quantifications of relative protein expression levels of Cyclin B1 (left) and Cyclin B2 (right) in GV-arrested oocytes from WT and ΔPAS3 mice from three biological replicates. Statistical significance was assessed using unpaired t-test (*** P ≤ 0.001, ns, not significant). ( C ) Overexpression of the intact Ccnb1 PAS1 short variant in WT oocytes causes premature meiotic cell cycle re-entry. WT oocytes were injected with an mRNA coding for PAS1 Ccnb1 short variant or a vehicle as a control. Timing of GVBD was assessed by time-lapse microscopy. Statistical significance was assessed using Mann–Whitney test (*** P ≤ 0.001, * P ≤ 0.05). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT + vehicle: 77.68 min, 95% confidence limit: 74.32–81.14; WT + Ccnb1 short: 57.38 min), as well as the slope of the curves (Hill coefficient: WT + vehicle: 4.0, WT + Ccnb1 short: 10). ( D ) Representative immunoblot showing the CDK1 activity in WT and ΔPAS3 oocytes 1 h after release from the cilostamide block (20 oocytes/lane). CDK1 activity was measured by phosphorylation level of the CDK1 substrate PP1 as detailed in the Materials and methods. Quantification of CDK1 activity levels between WT and PAS3 mutant from three biological replicates. Statistical significance was assessed using unpaired t -test (**** P ≤ 0.0001).

Techniques Used: Mutagenesis, Blocking Assay, MANN-WHITNEY, Western Blot, Expressing, Control, Over Expression, Variant Assay, Injection, Time-lapse Microscopy, Activity Assay, Phospho-proteomics

Altered MPF and ERK activities in ΔPAS3 mutant MII-stage oocytes. ( A ) Representative immunoblot showing CDK1 activity in WT and ΔPAS3 MII-stage oocytes (20 oocytes/lane). CDK1 activity was measured by the phosphorylation of the CDK1 substrate PP1 as detailed in the Materials and methods. ( B ) Quantification of CDK1 activity levels between WT and ΔPAS3 mutant from three biological replicates. Statistical significance was assessed using paired t -test (** P ≤ 0.01). ( C ) Representative immunoblot images of pERK1/2 protein levels in metaphase-II oocyte lysates from WT and ΔPAS3 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( D ) Quantifications of pERK1/2 in metaphase-II oocytes in WT and ΔPAS3 oocytes from four biological replicates. Statistical significance was calculated using unpaired t -test (* P ≤ 0.05). ( E ) Representative immunoblot images of Cyclin B1 protein levels in metaphase-II oocyte lysates from WT and ΔPAS3 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( F ) Quantifications of the relative protein levels of Cyclin B1 in metaphase-II oocytes in the WT and ΔPAS3 oocytes from four biological replicates. Statistical significance was reported using paired t-test.

Figure Legend Snippet: Altered MPF and ERK activities in ΔPAS3 mutant MII-stage oocytes. ( A ) Representative immunoblot showing CDK1 activity in WT and ΔPAS3 MII-stage oocytes (20 oocytes/lane). CDK1 activity was measured by the phosphorylation of the CDK1 substrate PP1 as detailed in the Materials and methods. ( B ) Quantification of CDK1 activity levels between WT and ΔPAS3 mutant from three biological replicates. Statistical significance was assessed using paired t -test (** P ≤ 0.01). ( C ) Representative immunoblot images of pERK1/2 protein levels in metaphase-II oocyte lysates from WT and ΔPAS3 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( D ) Quantifications of pERK1/2 in metaphase-II oocytes in WT and ΔPAS3 oocytes from four biological replicates. Statistical significance was calculated using unpaired t -test (* P ≤ 0.05). ( E ) Representative immunoblot images of Cyclin B1 protein levels in metaphase-II oocyte lysates from WT and ΔPAS3 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( F ) Quantifications of the relative protein levels of Cyclin B1 in metaphase-II oocytes in the WT and ΔPAS3 oocytes from four biological replicates. Statistical significance was reported using paired t-test.

Techniques Used: Mutagenesis, Western Blot, Activity Assay, Phospho-proteomics, Control

Image Search Results

Journal: EMBO Reports

Article Title: A phosphate-binding pocket in cyclin B3 is essential for XErp1/Emi2 degradation in meiosis I

doi: 10.1038/s44319-024-00347-8

Figure Lengend Snippet: Reagents and tools table

Article Snippet: Mouse anti-cyclin B2 , Santa Cruz , sc-53239.

Techniques: Recombinant, Plasmid Preparation, Expressing, Purification, Transduction, Western Blot, Sequencing, Concentration Assay, Protease Inhibitor, Software, Gel Extraction

Journal: Nucleic Acids Research

Article Title: Alternative cleavage and polyadenylation of the Ccnb1 mRNA defines accumulation of cyclin protein during the meiotic cell cycle

doi: 10.1093/nar/gkad1151

Figure Lengend Snippet: Loss of PAS1 Ccnb1 variant causes a delay in meiotic resumption. ( A ) Timing of GVBD in cultured denuded oocytes from WT and ΔPAS1 mutant mice. Oocytes were isolated as described in the Methods and timing of GVBD was scored by time-lapse microscopy after release from cilostamide block. Fifteen biological replicates for WT and six for the ΔPAS1 were included. Data were analyzed with non-parametric Mann–Whitney test and the calculated FDR was reported for each time point (* FDR ≤ 0.05; ** FDR ≤ 0.01; *** FDR ≤ 0.001). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT = 76.4 min, 95% confidence limit: 74.1–78.8; ΔPAS1 mutant = 107.4 min, 95% confidence limit: 96.2–120.1) as well as the slope of the curves (Hill coefficient: WT = 5.26, mutant = 3.99). ( B ) Timing of GVBD of individual oocytes from WT and ΔPAS1 mutant determined by time-lapse microscopy. Each point corresponded to one oocyte and the median of all determination was included. Statistical significance was calculated using unpaired t -test (**** P ≤ 0.0001). ( C ) Rescue of the PAS1 GVBD timing in ΔPAS1 oocytes. Denuded oocytes were microinjected with either vehicle (WT) or mRNA where the Ccnb1 ORF is fused to the intact PAS1 3′UTR ( Ccnb1 -PAS1 injected in ΔPAS1). The time when 50% of oocytes had undergone GVBD (Time 50% ) was comparable in the two groups (WT = 81.98 min; PAS1 rescue = 73.79). The two curves were not statistically different when using a Mann–Whitney test. ( D ) Representative immunoblots of Cyclin B1 and Cyclin B2 levels in lysates of GV oocytes from WT and ΔPAS1 mutant mice (150 oocytes/lane). DDB1 was used as a loading control. ( E , F ) Quantification of (D), relative protein levels of Cyclin B1 and Cyclin B2 in GV oocytes from WT and PAS1 mutant. Three biological replicates were included. Statistical significance was assessed using unpaired t -test (**** P ≤ 0.0001, ns, not significant).

Article Snippet: Following transfer, the membranes were blocked in Tris-buffered saline supplemented with 0.05% Tween 20 (TBST) containing 5% nonfat milk powder for 1 h at room temperature, then incubated at 4°C overnight with specific primary antibodies (1:1000 dilution) for the detection of the following proteins: Cyclin B1 (4138, Cell Signaling), Cyclin B2 (AF6004, R&D Systems), p-ERK1/2 (05–797R, EMD Millipore), and DDB1 (ab109027, Abcam).

Techniques: Variant Assay, Cell Culture, Mutagenesis, Isolation, Time-lapse Microscopy, Blocking Assay, MANN-WHITNEY, Injection, Western Blot, Control

Journal: Nucleic Acids Research

Article Title: Alternative cleavage and polyadenylation of the Ccnb1 mRNA defines accumulation of cyclin protein during the meiotic cell cycle

doi: 10.1093/nar/gkad1151

Figure Lengend Snippet: Loss of PAS1 Ccnb1 variant does not affect mouse oocyte progression to MII. ( A ) Time-lapse microscopy analysis of timing of the first polar body extrusion in WT and PAS1 mutant oocytes after release from cilostamide block. Experiments were repeated 6 times with oocytes retrieved from at least 1 mouse/experiment. The two curves were not statistically different when using a Mann–Whitney test. Time 50% : WT = 11.0 min, 95% confidence limit: 10.88–11.20; ΔPAS1 = 12.48 min, 95% confidence limit:12.23–12.75. ( B ) Violin plot of the duration of the first meiotic division in WT and ΔPAS1 oocytes. The duration of the first meiotic division was calculated by subtracting the time of GVBD from the time of PB1 extrusion. Statistical significance was assessed using Mann–Whitney test (ns, not significant). Number of oocytes used for the measurements: WT n = 286, ΔPAS1 n = 143. ( C ) Representative immunoblot images of Cyclin B1 and pERK1/2 protein levels in metaphase II oocyte lysates from WT and ΔPAS1 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( D ) Quantifications of relative protein expression levels of Cyclin B1 (left) and pERK1/2 (right) in metaphase II oocytes of WT and ΔPAS1 from four biological replicates. Statistical significance was calculated using unpaired t -test (ns, not significant).

Techniques: Variant Assay, Time-lapse Microscopy, Mutagenesis, Blocking Assay, MANN-WHITNEY, Western Blot, Control, Expressing

Journal: Nucleic Acids Research

Article Title: Alternative cleavage and polyadenylation of the Ccnb1 mRNA defines accumulation of cyclin protein during the meiotic cell cycle

doi: 10.1093/nar/gkad1151

Figure Lengend Snippet: Loss of PAS3 in the Ccnb1 3′ UTR leads to premature meiotic re-entry. ( A ) Time-lapse analysis of the timing of GVBD in WT and ΔPAS3 mutant oocytes after release from cilostamide block. Sixteen biological replicates for WT and five for the ΔPAS3 were included. Data were analyzed with non-parametric Mann–Whitney test and the calculated FDR was reported for each time point (*FDR ≤ 0.05; **FDR ≤ 0.01; ***FDR ≤ 0.001). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT = 76.06 min, 95% confidence limit: 72.6–79.6; ΔPAS3 = 50.20 min, 95% confidence limit: 47.92–52.63) as well as the slope of the curves (Hill coefficient: WT = 3.4, mutant = 7.8). ( B ) Representative immunoblot showing expression levels of Cyclin B1 and Cyclin B2 in WT and ΔPAS3 GV-stage oocyte lysates (150 oocytes/lane). DDB1 was used as a loading control. Quantifications of relative protein expression levels of Cyclin B1 (left) and Cyclin B2 (right) in GV-arrested oocytes from WT and ΔPAS3 mice from three biological replicates. Statistical significance was assessed using unpaired t-test (*** P ≤ 0.001, ns, not significant). ( C ) Overexpression of the intact Ccnb1 PAS1 short variant in WT oocytes causes premature meiotic cell cycle re-entry. WT oocytes were injected with an mRNA coding for PAS1 Ccnb1 short variant or a vehicle as a control. Timing of GVBD was assessed by time-lapse microscopy. Statistical significance was assessed using Mann–Whitney test (*** P ≤ 0.001, * P ≤ 0.05). A four-parameter logistic equation was used to calculate the time when 50% of oocytes had undergone GVBD (Time 50% : WT + vehicle: 77.68 min, 95% confidence limit: 74.32–81.14; WT + Ccnb1 short: 57.38 min), as well as the slope of the curves (Hill coefficient: WT + vehicle: 4.0, WT + Ccnb1 short: 10). ( D ) Representative immunoblot showing the CDK1 activity in WT and ΔPAS3 oocytes 1 h after release from the cilostamide block (20 oocytes/lane). CDK1 activity was measured by phosphorylation level of the CDK1 substrate PP1 as detailed in the Materials and methods. Quantification of CDK1 activity levels between WT and PAS3 mutant from three biological replicates. Statistical significance was assessed using unpaired t -test (**** P ≤ 0.0001).

Techniques: Mutagenesis, Blocking Assay, MANN-WHITNEY, Western Blot, Expressing, Control, Over Expression, Variant Assay, Injection, Time-lapse Microscopy, Activity Assay, Phospho-proteomics

Journal: Nucleic Acids Research

Article Title: Alternative cleavage and polyadenylation of the Ccnb1 mRNA defines accumulation of cyclin protein during the meiotic cell cycle

doi: 10.1093/nar/gkad1151

Figure Lengend Snippet: Altered MPF and ERK activities in ΔPAS3 mutant MII-stage oocytes. ( A ) Representative immunoblot showing CDK1 activity in WT and ΔPAS3 MII-stage oocytes (20 oocytes/lane). CDK1 activity was measured by the phosphorylation of the CDK1 substrate PP1 as detailed in the Materials and methods. ( B ) Quantification of CDK1 activity levels between WT and ΔPAS3 mutant from three biological replicates. Statistical significance was assessed using paired t -test (** P ≤ 0.01). ( C ) Representative immunoblot images of pERK1/2 protein levels in metaphase-II oocyte lysates from WT and ΔPAS3 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( D ) Quantifications of pERK1/2 in metaphase-II oocytes in WT and ΔPAS3 oocytes from four biological replicates. Statistical significance was calculated using unpaired t -test (* P ≤ 0.05). ( E ) Representative immunoblot images of Cyclin B1 protein levels in metaphase-II oocyte lysates from WT and ΔPAS3 mutant (50 oocytes/lane). DDB1 was used as a loading control. ( F ) Quantifications of the relative protein levels of Cyclin B1 in metaphase-II oocytes in the WT and ΔPAS3 oocytes from four biological replicates. Statistical significance was reported using paired t-test.

Techniques: Mutagenesis, Western Blot, Activity Assay, Phospho-proteomics, Control

Figure 3. Cyclin B2 C-terminal MIM is required for its kinetochore localization.

Journal: EMBO reports

Article Title: Mad2 promotes Cyclin B2 recruitment to the kinetochore for guiding accurate mitotic checkpoint.

doi: 10.15252/embr.202154171

Figure Lengend Snippet: Figure 3. Cyclin B2 C-terminal MIM is required for its kinetochore localization.

Article Snippet: Immunoprecipitation samples were resolved by Western blotting using a mouse anti-Cyclin B2 antibody (Santa Cruz, sc-28303) and a mouse anti-Mad2 antibody (Santa Cruz, sc-47747).

Techniques:

Figure 6. Working model to account for Cyclin B2 localization and function in mitosis.

Journal: EMBO reports

Article Title: Mad2 promotes Cyclin B2 recruitment to the kinetochore for guiding accurate mitotic checkpoint.

doi: 10.15252/embr.202154171

Figure Lengend Snippet: Figure 6. Working model to account for Cyclin B2 localization and function in mitosis.

Article Snippet: Immunoprecipitation samples were resolved by Western blotting using a mouse anti-Cyclin B2 antibody (Santa Cruz, sc-28303) and a mouse anti-Mad2 antibody (Santa Cruz, sc-47747).

Techniques:

A Volcano plot for the differential expressed genes affected by Pontin knockdown screened by RNA-seq with FC > 2 and FDR < 0.05. B GSEA plot indicated a significant correlation between Pontin and E2F target expressions. C Heatmap of the top 33 E2F1 targets expressions in U87MG cells affected by Pontin knockdown. D qRT-PCR detection of Pontin , E2F1 , AURKA , CDK1 , CDK4 , CCNA2 , CCNB2 , and E2F8 expressions in U87MG cells as transfected in Fig. . E Western blot analyses of E2F1, CDK1, CDK4, and Cyclin B2 expressions in U87MG cells as transfected in Fig. . Experiments in ( D ) and ( E ) were performed at least in triplicate. Data in ( D ) are presented as the mean ± SD. ns > 0.05; ** P < 0.01; *** P < 0.001.

Journal: Cell Death & Disease

Article Title: The ATPase Pontin is a key cell cycle regulator by amplifying E2F1 transcription response in glioma

doi: 10.1038/s41419-021-03421-4

Figure Lengend Snippet: A Volcano plot for the differential expressed genes affected by Pontin knockdown screened by RNA-seq with FC > 2 and FDR < 0.05. B GSEA plot indicated a significant correlation between Pontin and E2F target expressions. C Heatmap of the top 33 E2F1 targets expressions in U87MG cells affected by Pontin knockdown. D qRT-PCR detection of Pontin , E2F1 , AURKA , CDK1 , CDK4 , CCNA2 , CCNB2 , and E2F8 expressions in U87MG cells as transfected in Fig. . E Western blot analyses of E2F1, CDK1, CDK4, and Cyclin B2 expressions in U87MG cells as transfected in Fig. . Experiments in ( D ) and ( E ) were performed at least in triplicate. Data in ( D ) are presented as the mean ± SD. ns > 0.05; ** P < 0.01; *** P < 0.001.

Article Snippet: The primary antibodies used in Western blot were as follows: mouse anti-human Pontin (catalog SAB4200194; Sigma-aldrich, USA), mouse anti-human GAPDH (catalog BM3876; Boster, Wuhan, China), rabbit anti-human E2F1 (catalog 49286; Sabbiotech, USA), rabbit anti-human CDK1 (catalog 10762-1-AP; Proteintech, USA), rabbit anti-human CDK4 (catalog 12790 T; Cell Signaling Technology, USA), mouse anti-human cyclin B2 (catalog sc-28303; Santa Cruz Biotechnology, USA), mouse anti-flag tag (catalog F3165; Sigma-aldrich, USA).

Techniques: Knockdown, RNA Sequencing, Quantitative RT-PCR, Transfection, Western Blot

(A) Schematic of the regulation of substrate phosphorylation by Cdk1 and opposing phosphatases. Note that the Wee1 inhibitor PD0166285 compromises the positive and double-negative feedback loops that regulate the activity of Cdk1. (B) Schematic of the hysteresis experiment. Steady-state Cdk1 activity and substrate phosphorylation were measured as a function of non-degradable cyclin B1 (ΔN-Cyc B1) in the presence of the Wee1/Myt1 inhibitor PD0166285. The steady state was approached either starting from a state of low (interphase up; purple) or of high (M phase down; green) cyclin B concentration/Cdk1 activity. (C and D) Cdk1 activity as a function of ΔN-Cyc B1 concentration (as monitored by histone H1 phosphorylation) is graded and monostable in the presence of the Wee1/Myt1 inhibitor (5 μM PD0166285). Autoradiograph of the histone phosphorylation is shown in (C). Quantification of two technical duplicates (circles) for the measurement and the mean of the duplicates (connecting lines) is shown in (D). (E) The phosphorylation state of three Cdk1 substrates (APC3, Cdc25, and Nup53), monitored by mobility shift as a function of ΔN-Cyc B1 concentration. Note that despite the monostable response in Cdk1 activity shown in (C) and (D), these substrates still exhibit hysteretic responses. (F and G) Quantification of the APC3 hyperphosphorylation for the experiment in (E), plotted as a function of ΔN-Cyc B1 concentration (F) and as a function of the corresponding Cdk1 activities (G) as measured in (D). shows a summary of multiple experiments for this measurement. All activity and phosphorylation state analyses (C)–(G) were performed from the same experiment. See for a detailed characterization of the Wee1 inhibitor ( – ) and linearity tests for the antibodies .

Journal: Current biology : CB

Article Title: Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation

doi: 10.1016/j.cub.2020.11.058

Figure Lengend Snippet: (A) Schematic of the regulation of substrate phosphorylation by Cdk1 and opposing phosphatases. Note that the Wee1 inhibitor PD0166285 compromises the positive and double-negative feedback loops that regulate the activity of Cdk1. (B) Schematic of the hysteresis experiment. Steady-state Cdk1 activity and substrate phosphorylation were measured as a function of non-degradable cyclin B1 (ΔN-Cyc B1) in the presence of the Wee1/Myt1 inhibitor PD0166285. The steady state was approached either starting from a state of low (interphase up; purple) or of high (M phase down; green) cyclin B concentration/Cdk1 activity. (C and D) Cdk1 activity as a function of ΔN-Cyc B1 concentration (as monitored by histone H1 phosphorylation) is graded and monostable in the presence of the Wee1/Myt1 inhibitor (5 μM PD0166285). Autoradiograph of the histone phosphorylation is shown in (C). Quantification of two technical duplicates (circles) for the measurement and the mean of the duplicates (connecting lines) is shown in (D). (E) The phosphorylation state of three Cdk1 substrates (APC3, Cdc25, and Nup53), monitored by mobility shift as a function of ΔN-Cyc B1 concentration. Note that despite the monostable response in Cdk1 activity shown in (C) and (D), these substrates still exhibit hysteretic responses. (F and G) Quantification of the APC3 hyperphosphorylation for the experiment in (E), plotted as a function of ΔN-Cyc B1 concentration (F) and as a function of the corresponding Cdk1 activities (G) as measured in (D). shows a summary of multiple experiments for this measurement. All activity and phosphorylation state analyses (C)–(G) were performed from the same experiment. See for a detailed characterization of the Wee1 inhibitor ( – ) and linearity tests for the antibodies .

Article Snippet: The following antibodies were used for detection of the respective proteins: mouse α-Cdc27 (BD Biosciences, #610455), mouse α-cyclin B2 (Santa Cruz Biotechnology, #sc-53239), rabbit α-Nup53 serum, rabbit α-PPP1A pT320 (Abcam, #ab62334), rabbit α-Cdc25C, rabbit α-Wee1 pT150, rabbit α-Greatwall serum, rabbit α-ENSA serum, rabbit α-Arpp19, rabbit α-ENSA pS67/Arpp19 pS62 (Cell Signaling Technology, #5240) and rabbit α-Cdk1 pY15 (Cell Signaling Technology, #9111L).

Techniques: Phospho-proteomics, Activity Assay, Concentration Assay, Autoradiography, Mobility Shift

(A) Schematic of the system used to assess APC/C activity. ΔN-Cyc B1 titration experiments were performed as described in and steady-state APC/C activity was measured by following the degradation of a fluorescently labeled APC/C substrate (securin-CFP) using a plate reader. (B) APC/C is activated during mitosis. Significant loss of fluorescent signal was only detected in an M phase extract (red) but not in an interphase extract (blue) or in an extract not supplemented with securin-CFP (black). Shown is the mean (circles with connecting line) and the standard deviation (error band) of a technical triplicate. (C) Securin-CFP degradation dynamics after adding different concentrations of ΔN-Cyc B1, approaching steady state starting from either a state of high (M phase down; green) or low (interphase up; purple) cyclin B concentration/Cdk1 activity. Shown are data from two technical replicates (circles or squares; the dashed or solid lines, respectively, show the exponential fit of the data). Note that at intermediate concentrations of ΔN-Cyc B1 (10 or 15 nM), the steady-state level of APC/C activity depends upon whether the system has come from interphase or M phase. (D) Quantitation of the apparent first-order rate constant for APC/C activity plotted as a function of ΔN-Cyc B1 for the experiment shown in (C), including additional ΔN-Cyc B1 concentrations. Shown is the average of a technical duplicate with standard deviation. (E) Quantitation of the apparent first-order rate constant for APC/C activity (the same activities shown in D) plotted as a function of Cdk1 activity rather than non-degradable cyclin B concentration. Shown is the average of a technical duplicate with standard deviation. (F) Quantification of the apparent first-order rate constant for APC/C activity as a function of ΔN-Cyc B1. Shown are mean and standard error of the mean from 4 independent experiments (for 20 nM ΔN-Cyc B1: n = 3; for 40 nM ΔN-Cyc B1: n = 2). Note that due to variability between experiments, the switch-like transition between low and high APC/C activity is less obvious in the averaged data than it is in the given single experiment (D and E). All experiments were performed in the presence of 5 μM PD0166285.

Journal: Current biology : CB

Article Title: Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation

doi: 10.1016/j.cub.2020.11.058

Figure Lengend Snippet: (A) Schematic of the system used to assess APC/C activity. ΔN-Cyc B1 titration experiments were performed as described in and steady-state APC/C activity was measured by following the degradation of a fluorescently labeled APC/C substrate (securin-CFP) using a plate reader. (B) APC/C is activated during mitosis. Significant loss of fluorescent signal was only detected in an M phase extract (red) but not in an interphase extract (blue) or in an extract not supplemented with securin-CFP (black). Shown is the mean (circles with connecting line) and the standard deviation (error band) of a technical triplicate. (C) Securin-CFP degradation dynamics after adding different concentrations of ΔN-Cyc B1, approaching steady state starting from either a state of high (M phase down; green) or low (interphase up; purple) cyclin B concentration/Cdk1 activity. Shown are data from two technical replicates (circles or squares; the dashed or solid lines, respectively, show the exponential fit of the data). Note that at intermediate concentrations of ΔN-Cyc B1 (10 or 15 nM), the steady-state level of APC/C activity depends upon whether the system has come from interphase or M phase. (D) Quantitation of the apparent first-order rate constant for APC/C activity plotted as a function of ΔN-Cyc B1 for the experiment shown in (C), including additional ΔN-Cyc B1 concentrations. Shown is the average of a technical duplicate with standard deviation. (E) Quantitation of the apparent first-order rate constant for APC/C activity (the same activities shown in D) plotted as a function of Cdk1 activity rather than non-degradable cyclin B concentration. Shown is the average of a technical duplicate with standard deviation. (F) Quantification of the apparent first-order rate constant for APC/C activity as a function of ΔN-Cyc B1. Shown are mean and standard error of the mean from 4 independent experiments (for 20 nM ΔN-Cyc B1: n = 3; for 40 nM ΔN-Cyc B1: n = 2). Note that due to variability between experiments, the switch-like transition between low and high APC/C activity is less obvious in the averaged data than it is in the given single experiment (D and E). All experiments were performed in the presence of 5 μM PD0166285.

Techniques: Activity Assay, Titration, Labeling, Standard Deviation, Concentration Assay, Quantitation Assay

(A) Schematic of the regulation of PP2A-B55 activity by Cdk1 via Greatwall kinase (Gwl) and ENSA/Arpp19. Two double-negative feedback loops, a shorter one involving only PP2A-B55 and Arpp19/ENSA and a longer one involving Gwl kinase and PP2A-B55, could give rise to bistability. (B and C) The steady-state activity of PP2A-B55 is hysteretic in the presence of the Wee1/Myt1 inhibitor (10 μM PD0166285). Mitotic substrate phosphorylation (monitored by the mobility shift of Nup53) in (B) and PP2A-B55 activity in (C) are shown as a function of non-degradable cyclin B1 (ΔN-Cyc B1), approaching steady state from either a state of high (M phase down; green) or low (interphase up; purple) cyclin B concentration/Cdk1 activity (mean of technical duplicates with connecting line). Two additional experiments are shown in – . (D) Gwl and ENSA phosphorylation exhibit bistability in the presence of the Wee1/Myt1 inhibitor (5 μM PD0166285). Phosphorylation states of several Cdk1 substrates including Gwl and ENSA were analyzed by immunoblotting. shows an additional experiment. 10 μM Phos-tag was used to enhance the mobility shift upon ENSA phosphorylation. A shorter exposure for the ENSA immunoblot and a quantification of the phosphorylated form of ENSA are shown in and . An additional experiment is shown in and and an experiment detecting ENSA phosphorylation using a phospho-specific antibody against the phosphorylated S67 epitope of ENSA is shown in and . (E and F) Gwl kinase activity is ultrasensitive but not bistable. Cdk1 and Gwl kinase activities were measured for the experiment shown in (D) and are depicted as the dose response of Gwl kinase activity as a function of ΔN-Cyc B1 (E) or Cdk1 activity (F). Shown is the mean of a technical duplicate (circles). Although not bistable, the dose response of Gwl kinase activity exhibits significant ultrasensitivity as demonstrated by the large Hill exponent (n H ) necessary to fit the data (solid lines in E and F). Additional experiments are shown in – .

Journal: Current biology : CB

Article Title: Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation

doi: 10.1016/j.cub.2020.11.058

Figure Lengend Snippet: (A) Schematic of the regulation of PP2A-B55 activity by Cdk1 via Greatwall kinase (Gwl) and ENSA/Arpp19. Two double-negative feedback loops, a shorter one involving only PP2A-B55 and Arpp19/ENSA and a longer one involving Gwl kinase and PP2A-B55, could give rise to bistability. (B and C) The steady-state activity of PP2A-B55 is hysteretic in the presence of the Wee1/Myt1 inhibitor (10 μM PD0166285). Mitotic substrate phosphorylation (monitored by the mobility shift of Nup53) in (B) and PP2A-B55 activity in (C) are shown as a function of non-degradable cyclin B1 (ΔN-Cyc B1), approaching steady state from either a state of high (M phase down; green) or low (interphase up; purple) cyclin B concentration/Cdk1 activity (mean of technical duplicates with connecting line). Two additional experiments are shown in – . (D) Gwl and ENSA phosphorylation exhibit bistability in the presence of the Wee1/Myt1 inhibitor (5 μM PD0166285). Phosphorylation states of several Cdk1 substrates including Gwl and ENSA were analyzed by immunoblotting. shows an additional experiment. 10 μM Phos-tag was used to enhance the mobility shift upon ENSA phosphorylation. A shorter exposure for the ENSA immunoblot and a quantification of the phosphorylated form of ENSA are shown in and . An additional experiment is shown in and and an experiment detecting ENSA phosphorylation using a phospho-specific antibody against the phosphorylated S67 epitope of ENSA is shown in and . (E and F) Gwl kinase activity is ultrasensitive but not bistable. Cdk1 and Gwl kinase activities were measured for the experiment shown in (D) and are depicted as the dose response of Gwl kinase activity as a function of ΔN-Cyc B1 (E) or Cdk1 activity (F). Shown is the mean of a technical duplicate (circles). Although not bistable, the dose response of Gwl kinase activity exhibits significant ultrasensitivity as demonstrated by the large Hill exponent (n H ) necessary to fit the data (solid lines in E and F). Additional experiments are shown in – .

Techniques: Activity Assay, Phospho-proteomics, Mobility Shift, Concentration Assay, Western Blot

(A) Okadaic acid (OA) was used to partially inhibit the activity of PP2A-B55 and the feedback between PP2A-B55 and ENSA/Arpp19. (B and C) The dose-response relationship of the phosphorylation state of the APC/C subunit APC3 as a function of ΔN-Cyc B1, approaching steady state starting from either a state of high (M phase down) or low (interphase up) cyclin B concentration/Cdk1 activity in the presence of the Wee1/Myt1 inhibitor (25 μM PD0166285) and in the absence (DMSO) or presence (OA) of different concentrations of OA. OA decreased the hysteresis seen in the DMSO control and made intermediate phosphorylation states more apparent. Note that the DMSO and OA comparisons were performed in parallel using the same extract, but (B) and (C) were performed using different extracts; biological variability may account for the differences in the overall response between the two DMSO control experiments. (D) Thiophosphorylated Arpp19 (Arpp19-S) was used to partially inhibit the activity of PP2A-B55 and the feedback between PP2A-B55 and ENSA/Arpp19. (E and F) The dose-response relationship of the phosphorylation state of Nup53 as a function of ΔN-Cyc B1, approaching steady state starting from either a state of high (M phase down) or low (interphase up) cyclin B concentration/Cdk1 activity in the presence of the Wee1/Myt1 inhibitor (10 μM PD0166285) and in the absence (DMSO) or presence (Arpp19-S) of different concentrations of Arpp19-S. Arpp19-S decreased the hysteresis seen in the DMSO control and made intermediate phosphorylation states more apparent. Note that the DMSO and Arpp19-S comparison was performed in parallel using the same extract, but for (E) and (F) was performed using different extracts; biological variability may account for the differences in the overall response between the two DMSO control experiments, and variability in the activity of the ΔN-Cyc B1 preparation might account for overall differences in the response curve when comparing (C) and (D) to (E) and (F). See also .

Journal: Current biology : CB

Article Title: Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation

doi: 10.1016/j.cub.2020.11.058

Figure Lengend Snippet: (A) Okadaic acid (OA) was used to partially inhibit the activity of PP2A-B55 and the feedback between PP2A-B55 and ENSA/Arpp19. (B and C) The dose-response relationship of the phosphorylation state of the APC/C subunit APC3 as a function of ΔN-Cyc B1, approaching steady state starting from either a state of high (M phase down) or low (interphase up) cyclin B concentration/Cdk1 activity in the presence of the Wee1/Myt1 inhibitor (25 μM PD0166285) and in the absence (DMSO) or presence (OA) of different concentrations of OA. OA decreased the hysteresis seen in the DMSO control and made intermediate phosphorylation states more apparent. Note that the DMSO and OA comparisons were performed in parallel using the same extract, but (B) and (C) were performed using different extracts; biological variability may account for the differences in the overall response between the two DMSO control experiments. (D) Thiophosphorylated Arpp19 (Arpp19-S) was used to partially inhibit the activity of PP2A-B55 and the feedback between PP2A-B55 and ENSA/Arpp19. (E and F) The dose-response relationship of the phosphorylation state of Nup53 as a function of ΔN-Cyc B1, approaching steady state starting from either a state of high (M phase down) or low (interphase up) cyclin B concentration/Cdk1 activity in the presence of the Wee1/Myt1 inhibitor (10 μM PD0166285) and in the absence (DMSO) or presence (Arpp19-S) of different concentrations of Arpp19-S. Arpp19-S decreased the hysteresis seen in the DMSO control and made intermediate phosphorylation states more apparent. Note that the DMSO and Arpp19-S comparison was performed in parallel using the same extract, but for (E) and (F) was performed using different extracts; biological variability may account for the differences in the overall response between the two DMSO control experiments, and variability in the activity of the ΔN-Cyc B1 preparation might account for overall differences in the response curve when comparing (C) and (D) to (E) and (F). See also .

Techniques: Activity Assay, Phospho-proteomics, Concentration Assay, Control, Comparison

$(A–C) Phosphorylation and dephosphorylation of Cdk1 substrates show a distinct time lag compared to the increase and decrease in cyclin B concentration and Cdk1 activity. The changes in Cdk1 activity (B and C; mean of a technical duplicate), cyclin B2 concentration (A and C), and the phosphorylation of several substrates (B) were measured with high temporal resolution in a cycling extract progressing through mitosis. Note that cyclin B2 and Cdk1 activity are minimal at 61 min whereas most substrates are still hyperphosphorylated (B and C; for Cdk1 activity and the phosphospecies [as a fraction of total signal], exponential decays were fitted to the declining part of the time course). (D and E) PP2A-B55 activity peaks prior to mitotic entry and during mitotic exit. The phosphorylation of two mitotic substrates (D; quantification for Nup53 and PP1 T320 is shown in E in orange and green, respectively) as well as the concentration of cyclin B2 (D) and the activity of Cdk1 and PP2A-B55 (E; black and blue, respectively) were measured in a cycling extract progressing through mitosis. For the PP2A-B55 measurements, the assays were carried out on undiluted extracts; thus, the PP2A-B55 activity could be changing during the 3 min the phosphatase assay is performed. Accordingly, we have plotted the time of each PP2A-B55 measurement as the middle of this incubation period and show the range of the assay time as a horizontal line. Note that in contrast to PP2A-B55 activity, PP1 T320 phosphorylation closely follows the activity of Cdk1 (D and E). An additional independent experiment is shown in , , , and .$

Journal: Current biology : CB

Article Title: Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation

doi: 10.1016/j.cub.2020.11.058

Figure Lengend Snippet: (A–C) Phosphorylation and dephosphorylation of Cdk1 substrates show a distinct time lag compared to the increase and decrease in cyclin B concentration and Cdk1 activity. The changes in Cdk1 activity (B and C; mean of a technical duplicate), cyclin B2 concentration (A and C), and the phosphorylation of several substrates (B) were measured with high temporal resolution in a cycling extract progressing through mitosis. Note that cyclin B2 and Cdk1 activity are minimal at 61 min whereas most substrates are still hyperphosphorylated (B and C; for Cdk1 activity and the phosphospecies [as a fraction of total signal], exponential decays were fitted to the declining part of the time course). (D and E) PP2A-B55 activity peaks prior to mitotic entry and during mitotic exit. The phosphorylation of two mitotic substrates (D; quantification for Nup53 and PP1 T320 is shown in E in orange and green, respectively) as well as the concentration of cyclin B2 (D) and the activity of Cdk1 and PP2A-B55 (E; black and blue, respectively) were measured in a cycling extract progressing through mitosis. For the PP2A-B55 measurements, the assays were carried out on undiluted extracts; thus, the PP2A-B55 activity could be changing during the 3 min the phosphatase assay is performed. Accordingly, we have plotted the time of each PP2A-B55 measurement as the middle of this incubation period and show the range of the assay time as a horizontal line. Note that in contrast to PP2A-B55 activity, PP1 T320 phosphorylation closely follows the activity of Cdk1 (D and E). An additional independent experiment is shown in , , , and .

Techniques: Phospho-proteomics, De-Phosphorylation Assay, Concentration Assay, Activity Assay, Phosphatase Assay, Incubation

Journal: Current biology : CB

Article Title: Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation

doi: 10.1016/j.cub.2020.11.058

Figure Lengend Snippet:

Techniques: Recombinant, Protease Inhibitor, Expressing, Software

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